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Updated: Jul 5, 2026

Colorectal Cancer Cell Surface Protein Profiling Using an Antibody Microarray and Fluorescence Multiplexing

Colorectal Cancer Cell Surface Protein Profiling Using an Antibody Microarray and Fluorescence Multiplexing

Published on: September 25, 2011

Cell-based mucin arrays.

Felix Goerdeler¹, Yoshiki Narimatsu¹, Christian Büll²

¹Department of Cellular and Molecular Medicine, Faculty of Health Sciences, Copenhagen Center for Glycomics & Center for Glycocalyx Research, University of Copenhagen,Copenhagen, Denmark.

Methods in Enzymology

|July 3, 2026

Summary

This summary is machine-generated.

A novel cell-based mucin array platform allows researchers to study how O-glycan structures and patterns on mucins affect biological interactions. This tool enables detailed analysis of mucin-glycan binding and degradation by microbes and immune receptors.

Keywords:

Mucins O-glycans Siglecs mucin-binding proteins mucinases

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Last Updated: Jul 5, 2026

Colorectal Cancer Cell Surface Protein Profiling Using an Antibody Microarray and Fluorescence Multiplexing

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Fabrication of a Multiplexed Artificial Cellular MicroEnvironment Array

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Area of Science:

Glycoscience
Cell Biology
Biochemistry

Background:

Mucins are key glycoproteins involved in diverse biological processes.
Understanding mucin O-glycan structure and function is crucial for deciphering cell-surface interactions.
Current methods often fail to replicate the native context of mucin O-glycans.

Purpose of the Study:

To introduce and describe a versatile cell-based mucin array platform.
To enable the study of mucin O-glycan structures in their native protein context.
To investigate mucin interactions with various binding partners and enzymes.

Main Methods:

Development of glycoengineered mammalian cell lines (HEK293/CHO) to control O-glycan display.
Creation of recombinant mucin reporters mimicking natural mucin domains or artificial Glycocarriers.
Application of the platform in bioassays for studying glycan/mucin binding and enzymatic degradation.

Main Results:

The platform successfully displays customized O-glycan structures with defined sialylation, fucosylation, and sulfation.
It preserves the native protein context, allowing investigation of O-glycan density, clustering, and multivalency.
The array was used to probe binding by viral/microbial adhesins and human Siglec receptors, and to analyze mucinase activity.

Conclusions:

The cell-based mucin array is a powerful tool for dissecting mucin-glycan interactions and mucin degradation.
It overcomes limitations of existing technologies by preserving clustered and patterned O-glycan contexts.
This platform facilitates a deeper understanding of mucin biology in health and disease.